BMRB Entry 50233
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50233
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Title: Model-free analysis of 15N spin-relaxation data for TRBP2-dsRBD1 PubMed: 35134335
Deposition date: 2020-04-14 Original release date: 2022-02-16
Authors: Paithankar, Harshad; Chugh, Jeetender
Citation: Paithankar, Harshad; Tarang, Guneet Singh; Parvez, Firdousi; Marathe, Aniket; Joshi, Manali; Chugh, Jeetender. "Relay of intrinsic microsecond timescale conformational dynamics observed in an RNA-binding domain of TRBP upon enthalpy-driven binding of dsRNA" Biophys. J. ., .-. (2022).
Assembly members:
entity_1, polymer, 108 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pSV272
Entity Sequences (FASTA):
entity_1: GGAMSEEEQGSGTTTGCGLP
SIEQMLAANPGKTPISLLQE
YGTRIGKTPVYDLLKAEGQA
HQPNFTFRVTVGDTSCTGQG
PSKKAAKHKAAEVALKHLKG
GSMLEPAL
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
Data type | Count |
T1 relaxation values | 138 |
T2 relaxation values | 138 |
heteronuclear NOE values | 138 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | TRBP2-dsRBD1 | 1 |
Entities:
Entity 1, TRBP2-dsRBD1 108 residues - Formula weight is not available
N-terminal residues GGA are non-native to the protein and are left after the cleavage of the fusion tag using protease.
1 | GLY | GLY | ALA | MET | SER | GLU | GLU | GLU | GLN | GLY | ||||
2 | SER | GLY | THR | THR | THR | GLY | CYS | GLY | LEU | PRO | ||||
3 | SER | ILE | GLU | GLN | MET | LEU | ALA | ALA | ASN | PRO | ||||
4 | GLY | LYS | THR | PRO | ILE | SER | LEU | LEU | GLN | GLU | ||||
5 | TYR | GLY | THR | ARG | ILE | GLY | LYS | THR | PRO | VAL | ||||
6 | TYR | ASP | LEU | LEU | LYS | ALA | GLU | GLY | GLN | ALA | ||||
7 | HIS | GLN | PRO | ASN | PHE | THR | PHE | ARG | VAL | THR | ||||
8 | VAL | GLY | ASP | THR | SER | CYS | THR | GLY | GLN | GLY | ||||
9 | PRO | SER | LYS | LYS | ALA | ALA | LYS | HIS | LYS | ALA | ||||
10 | ALA | GLU | VAL | ALA | LEU | LYS | HIS | LEU | LYS | GLY | ||||
11 | GLY | SER | MET | LEU | GLU | PRO | ALA | LEU |
Samples:
sample_1: TRBP2-dsRBD1, [U-100% 15N], 1.8 mM; D2O, [U-2H], 10%; DTT 1 mM; sodium phosphate 10 mM; sodium chloride 100 mM; EDTA 1 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6.4; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
T1/R1 relaxation | sample_1 | isotropic | sample_conditions_1 |
T2/R2 relaxation | sample_1 | isotropic | sample_conditions_1 |
1H-15N heteronoe | sample_1 | isotropic | sample_conditions_1 |
T1/R1 relaxation | sample_1 | isotropic | sample_conditions_1 |
T2/R2 relaxation | sample_1 | isotropic | sample_conditions_1 |
1H-15N heteronoe | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.5 - collection
NMRPipe - processing
NMRFAM-SPARKY - peak picking
Relax v4.0.3 - data analysis
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 750 MHz